Enhancing the Peroxygenase Activity of a Cofactor-Independent Peroxyzyme by Directed Evolution Enabling Gram-Scale Epoxide Synthesis

Chemistry. 2022 Oct 21;28(59):e202201651. doi: 10.1002/chem.202201651. Epub 2022 Aug 26.

Abstract

Peroxygenases selectively incorporate oxygen into organic molecules making use of the environmentally friendly oxidant H2 O2 with water being the sole by-product. These biocatalysts can provide 'green' routes for the synthesis of enantioenriched epoxides, which are fundamental intermediates in the production of pharmaceuticals. The peroxyzyme 4-oxalocrotonate tautomerase (4-OT), catalysing the epoxidation of a variety of α,β-unsaturated aldehydes with H2 O2 , is outstanding because of its independence from any cost-intensive cofactor. However, its low-level peroxygenase activity and the decrease in the enantiomeric excess of the corresponding α,β-epoxy-aldehydes under preparative-scale conditions is limiting the potential of 4-OT. Herein we report the directed evolution of a tandem-fused 4-OT variant, which showed an ∼150-fold enhanced peroxygenase activity compared to 4-OT wild type, enabling the synthesis of α,β-epoxy-aldehydes in milligram- and gram-scale with high enantiopurity (up to 98 % ee) and excellent conversions. This engineered cofactor-independent peroxyzyme can provide new opportunities for the eco-friendly and practical synthesis of enantioenriched epoxides at large scale.

Keywords: cofactor-independent; directed evolution; epoxidation; peroxygenase; peroxyzyme.

MeSH terms

  • Aldehydes*
  • Epoxy Compounds*
  • Oxidants
  • Oxygen
  • Pharmaceutical Preparations
  • Water

Substances

  • peroxygenase
  • Epoxy Compounds
  • Aldehydes
  • Oxygen
  • Water
  • Oxidants
  • Pharmaceutical Preparations